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Literature summary extracted from

  • Kralj, S.; Grijpstra, P.; van Leeuwen, S.S.; Leemhuis, H.; Dobruchowska, J.M.; van der Kaaij, R.M.; Malik, A.; Oetari, A.; Kamerling, J.P.; Dijkhuizen, L.
    4,6-alpha-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70 (2011), Appl. Environ. Microbiol., 77, 8154-8163.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.B34 expression in Esdcherichia coli Limosilactobacillus reuteri

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.B34 D1015N mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose) Limosilactobacillus reuteri
2.4.1.B34 D1015N mutation in putative nucleophile, mutant shows no activity on maltooligosaccharides Limosilactobacillus reuteri

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.B34 Limosilactobacillus reuteri
-
-
-
2.4.1.B34 Limosilactobacillus reuteri Q5SBM0
-
-
2.4.1.B34 Limosilactobacillus reuteri DSM 20016
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.B34
-
 Limosilactobacillus reuteri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.B34 amylose + maltose the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages Limosilactobacillus reuteri maltotriose + panose panose i.e. Glc-alpha-(1->6)-maltose ?
2.4.1.B34 amylose + maltose the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages Limosilactobacillus reuteri DSM 20016 maltotriose + panose panose i.e. Glc-alpha-(1->6)-maltose ?
2.4.1.B34 Maltoheptaose the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 Maltoheptaose the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products Limosilactobacillus reuteri DSM 20016 ?
-
 ?
2.4.1.B34 maltoheptaose + H2O
-
 Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 maltohexaose + H2O
-
 Limosilactobacillus reuteri D-glucose + maltopentaose first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20% ?
2.4.1.B34 maltooligosaccharide the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 maltooligosaccharide the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products Limosilactobacillus reuteri DSM 20016 ?
-
 ?
2.4.1.B34 maltopentaose + H2O
-
 Limosilactobacillus reuteri D-glucose + maltotetraose first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20% ?
2.4.1.B34 Maltotetraose
-
 Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 additional information the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 additional information enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 additional information no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides Limosilactobacillus reuteri ?
-
 ?
2.4.1.B34 additional information the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose Limosilactobacillus reuteri DSM 20016 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.B34 GTFB protein
-
 Limosilactobacillus reuteri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.B34 30 37 substrate: maltotetraose Limosilactobacillus reuteri
2.4.1.B34 37
-
-
 Limosilactobacillus reuteri
2.4.1.B34 37
-
 assay at Limosilactobacillus reuteri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.B34 4 5 substrate: maltotetraose Limosilactobacillus reuteri
2.4.1.B34 4.7
-
-
 Limosilactobacillus reuteri
2.4.1.B34 4.7
-
 assay at Limosilactobacillus reuteri